{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,3,26]],"date-time":"2024-03-26T02:42:07Z","timestamp":1711420927480},"reference-count":41,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2009,2,10]],"date-time":"2009-02-10T00:00:00Z","timestamp":1234224000000},"content-version":"vor","delay-in-days":4303,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["bpspubs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["British J Pharmacology"],"published-print":{"date-parts":[[1997,5]]},"abstract":"<jats:p>\n<jats:list list-type=\"explicit-label\">\n<jats:list-item><jats:p>The ability of acetylshikonin to inhibit the respiratory burst in rat neutrophils was characterized and the underlying mechanism of action was also assessed in the present study.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>Acetylshikonin caused an irreversible and a concentration\u2010dependent inhibition of formylmethionyl\u2010leucyl\u2010phenylalanine (fMLP) plus dihydrocytochalasin B (CB)\u2010 and phorbol 12\u2010myristate 13\u2010acetate (PMA)\u2010induced superoxide anion (O<jats:sub>2<\/jats:sub><jats:sup>.\u2212<\/jats:sup>) generation with IC<jats:sub>50<\/jats:sub> values of 0.48\u00b10.03 and 0.39\u00b10.03\u2003\u03bc<jats:sc>M<\/jats:sc>, respectively. Acetylshikonin also inhibited the O<jats:sub>2<\/jats:sub> consumption in neutrophils in response to fMLP\/CB as well as to PMA.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>Acetylshikonin did not scavenge the generated O<jats:sub>2<\/jats:sub><jats:sup>.\u2212<\/jats:sup> in the xanthine\u2010xanthine oxidase system or during dihydroxyfumaric acid (DHF) autoxidation but, on the contrary, acetylshikonin enhanced the O<jats:sub>2<\/jats:sub><jats:sup>.\u2212<\/jats:sup> generation in these cell\u2010free oxygen radical generating systems.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>Acetylshikonin inhibited the formation of inositol trisphosphate (IP<jats:sub>3<\/jats:sub>) (39.0\u00b17.8% inhibition at 10\u2003\u03bc<jats:sc>M<\/jats:sc>, <jats:italic>P<\/jats:italic>&lt;0.05) in neutrophils in response to fMLP.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>Both the neutrophil cytosolic protein kinase C (PKC) activity and the PMA\u2010induced PKC associated with the membrane were unaffected by acetylshikonin.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>Acetylshikonin did not affect the porcine heart protein kinase A (PKA) activity. Upon exposure to acetylshikonin, the cellular cyclic AMP level was decreased in neutrophils in response to fMLP.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The cellular formation of phosphatidic acid (PA) and, in the presence of ethanol, phosphatidylethanol (PEt) induced by fMLP\/CB were inhibited by acetylshikonin (60.1\u00b17.3 and 63.2\u00b110.5% inhibition, respectively, at 10\u2003\u03bc<jats:sc>M<\/jats:sc>, both <jats:italic>P<\/jats:italic>&lt;0.05). Moreover, acetylshikonin attenuated the fMLP\/CB\u2010induced protein tyrosine phosphorylation (about 90% inhibition at 1\u2003\u03bc<jats:sc>M<\/jats:sc>).<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>In PMA\u2010activated neutrophil particulate NADPH oxidase preparations, acetylshikonin did not inhibit, but enhanced, the O<jats:sub>2<\/jats:sub><jats:sup>.\u2212<\/jats:sup> generation in the presence of NADPH. However, acetylshikonin decreased the membrane associated p47<jats:sup><jats:italic>phox<\/jats:italic><\/jats:sup> in PMA\u2010activated neutrophils (about 60% inhibition at 1\u2003\u03bc<jats:sc>M<\/jats:sc>).<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>Collectively, these results suggest that the attenuation of protein tyrosine phosphorylation and a failure in the assembly of a functional NADPH oxidase complex probably contribute predominantly to the inhibition of respiratory burst in neutrophils by acetylshikonin. In contrast, the blockade of phospholipase C (PLC) and phospholipase D (PLD) pathways play only a minor role in this respect.<\/jats:p><\/jats:list-item>\n<\/jats:list>\n<\/jats:p>","DOI":"10.1038\/sj.bjp.0701147","type":"journal-article","created":{"date-parts":[[2006,7,21]],"date-time":"2006-07-21T14:37:20Z","timestamp":1153492640000},"page":"409-416","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":24,"title":["Investigation of the inhibition by acetylshikonin of the respiratory burst in rat neutrophils"],"prefix":"10.1111","volume":"121","author":[{"given":"Jih P.","family":"Wang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lo T.","family":"Tsao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shue L.","family":"Raung","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mei F.","family":"Hsu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sheng C.","family":"Kuo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2009,2,10]]},"reference":[{"key":"e_1_2_5_2_1","doi-asserted-by":"publisher","DOI":"10.1021\/jm00006a025"},{"key":"e_1_2_5_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)45614-1"},{"key":"e_1_2_5_4_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.49.070180.003403"},{"key":"e_1_2_5_5_1","doi-asserted-by":"crossref","first-page":"8210","DOI":"10.1016\/S0021-9258(18)68464-9","article-title":"Activation of NADPH\u2010dependent superoxide production in plasma membrane extracts of pig neutrophils by phosphatidic acid","volume":"263","author":"Bellavite P.","year":"1988","journal-title":"J. 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